Catalog # CP1151


Cofilin 1 (Ser-3), phospho-specific

Rabbit Polyclonal

Application Dilution
ELISA1:2000
ICC1:50
WB1:1000

Size 100 μl

Species Reactivity Hu, Rt, Ms, Ck

MW 19 kDa

$295

Members of the ADF/cofilin (AC) family are actin-severing proteins that regulate actin remodeling during cellular events such as cell migration, cytokinesis, phagocytosis, endocytosis, axon development, and immune cell activation. In mammals, there are three members of the AC family, muscle-specific cofilin (Cofilin 2), non-muscle cofilin (Cofilin 1), and ADF. In humans, cofilin 1 and ADF have 72% identity, with the major amino acid differences found in the C-terminal region. Regulation of cofilin activity can occur through serine phosphorylation. Activation of cofilin kinases, LIMK1 or LIMK2, leads to phosphorylation of cofilin at serine 3. This phosphorylation disrupts cofilin binding to actin in vitro and in vivo. Multiple phosphatases, PP1, PP2A, PP2B, slingshot, and chronophin can dephosphorylate Ser-3 and activate actin binding. Thus, Ser-3 phosphorylation is a major site for the regulation of cofilin activity.

 

References

Maciver, S.K. & Hussey, P.J. (2002). Genome Biol. 3(5):3007.
Aizawa, H., et al. (2001). Nature Neurosci. 4(4):367.
Bamburg, J.R. (1999). Annu Rev Cell Dev Biol. 15:185.

A synthetic phospho-peptide (coupled to KLH) corresponding to amino acid residues surrounding serine 3 in human Cofilin 1. This sequence has 100% homology with similar regions of rat and mouse Cofilin 1, and has two amino acid differences from human Cofilin 2.

*For more information, see UniProt Accession P23528
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.

The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.

This antibody was cross-adsorbed to unphosphorylated Coflin 1 peptide then affinity purified using phospho-Cofilin 1 (Ser-3) peptide (without carrier). The antibody detects a 19 kDa* protein corresponding to the molecular mass of phosphorylated Cofilin 1 on SDS-PAGE immunoblots of Jurkat cells. This band can be removed by lambda phosphatase treatment.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.

Western blot of cofilin in jurkat cells. The blots were untreated (lanes 1 & 4) or treated (lanes 2, 3, 5 & 6) with lambda phosphatase. In lanes 3 & 6, the phosphatase was inhibited with phospho-Cofilin 1 (Ser-3) peptide. The blots were probed with anti-Cofilin 1 (Ser-3) phospho-specific (lanes 1-3) or anti-Cofilin 1 (N-terminus) (lanes 4-6).

Immunocytochemical labeling in chick dorsal root ganglion neurons using anti-Cofilin (N-terminus; CP1131), anti-Cofilin (Ser-3; CP1151), anti-βIII-Tubulin (C-terminus; TP1691) and anti-β-Tubulin (TM1541) antibodies. (Images provided by Dr. Diane Snow, Department of Anatomy & Neurobiology, University of Kentucky).



This kit contains:

KIT SUMMARY